› 3he8

X-ray diffraction
1.9Å resolution

Structural study of Clostridium thermocellum Ribose-5-Phosphate Isomerase B

Released:
DOI: 10.2210/pdb3he8/pdb
Model geometry
Fit model/data
PDB entry 3he8 coloured by chain, front view.
PDB entry 3he8 coloured by chain, side view.
PDB entry 3he8 coloured by chain, top view.
Source organism: Acetivibrio thermocellus ATCC 27405
Primary publication:
Crystal structure of Clostridium thermocellum ribose-5-phosphate isomerase B reveals properties critical for fast enzyme kinetics.
Jung J, Kim JK, Yeom SJ, Ahn YJ, Oh DK, Kang LW
Appl Microbiol Biotechnol 90 517-27 (2011)
PMID: 21253719

Function and Biology Details

Reaction catalysed: 
D-ribose 5-phosphate = D-ribulose 5-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-107074 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sugar-phosphate isomerase, RpiB/LacA/LacB family Chains: A, B
Molecule details ›
Chains: A, B
Length: 149 amino acids
Theoretical weight: 16.15 KDa
Source organism: Acetivibrio thermocellus ATCC 27405
Expression system: Escherichia coli
UniProt:
  • Canonical: A3DIL8 (Residues: 1-149; Coverage: 100%)
Gene name: Cthe_2597
Sequence domains: Ribose/Galactose Isomerase
Structure domains: Sugar-phosphate isomerase, RpiB/LacA/LacB

Ligands and Environments

1 bound ligand:
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: PAL/PLS BEAMLINE 6C1
Spacegroup: P3221
Unit cell:
a: 69.515Å b: 69.515Å c: 154.434Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.189 0.188 0.22
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Microbial metabolism and biotechnological production of D-allose.
Lim et al. (2011)
1 more

1 mention without citation

The Blueprint of a Minimal Cell: MiniBacillus.
Reuß et al. (2016)